The microstructures and mechanical properties of T92 martensitic steel/Super304 austenitic steel weld joints with three welding consumables were investigated. Three types of welding materials ERNiCr-3, ERNiCrCoMo-1and T-304H were utilized to obtain dissimilar welds by using gas tungsten arc weld (GTAW). The results show that heat affect zone (HAZ) of T92 steel consists of coarse-grained and fine-grained tempered martensites. The microstructures of joints produced from ERNiCrCoMo-1 consist of equiaxed dendrite and columnar dendrite grains, which are more complicated than that of ERNiCr-3. In the tensile tests, joints constructed from ERNiCrCoMo-1 and T-304H met the ASME standard. The highest fracture energy was observed in specimens with the welding material ERNiCrCoMo-1. Ni content in weld seam of ERNiCrCoMo-1 was highest, which was above 40%. In conclusion, the nickel alloy ERNiCrCoMo-1 was the most suitable welding material for joints produced from T92 martensitic steel/Super304 austenitic steel.
To keep genetic diversity, flowering plants have developed a self-incompatibility system, which can prevent self-pollination. It has been reported that calcium concentration in pistil papilla cells was increased after self-pollination in transformed self-incompatible Arabidopsis thaliana. In this study, we found that CML27 changed its expression level for both mRNA and protein when compared to transcriptome and proteome. At the same time, CML27 was expressed in the anther and pistil at a high level and reached up to 5-fold up-regulated expression in the pistil at 1 h post-pollination when compared to 0 min. In order to find out potential proteins that may interact with BoCML27, BoCML27 was expressed in and isolated from E. coli. After its co-incubation with Brassica oleracea pistil proteins, the products were separated on SDS-PAGE gels. We found a specific band at the position between 130–180 kDa. Through LC-MS-MS (Q-TOF) analysis, eight proteins were identified from the band. The proteins include 26S proteasome non-ATPase regulatory (26S), Phospholipase D, alpha 2 (PLDα2) involved in Ca2+ binding and Coatomer subunit alpha-2-like (Coatomer) involved in vesicle mediated transport. All of these identified proteins provide new insights for the self-incompatibility response in B. oleracea, specific for increasing Ca2+ concentration in pistil papilla cells.
The data aggregation process of wireless sensor networks faces serious security problems. In order to defend the internal attacks launched by captured nodes and ensure the reliability of data aggregation, a secure data aggregation mechanism based on constrained supervision is proposed for wireless sensor network, which uses the advanced LEACH clustering method to select cluster heads. Then the cluster heads supervise the behaviors of cluster members and evaluate the trust values of nodes according to the communication behavior, data quality and residual energy. Then the node with the highest trust value is selected as the supervisor node to audit the cluster head and reject nodes with low trust values. Results show that the proposed mechanism can effectively identify the unreliable nodes, guarantee the system security and prolong the network lifetime.
Sapelovirus A (SV-A) is a positive-sense single-stranded RNA virus which is associated with acute diarrhea, pneumonia and reproductive disorders. The virus capsid is composed of four proteins, and the functions of the structural proteins are unclear. In this study, we expressed SV-A structural protein VP1 and studied its antigenicity and immunogenicity. SDS-PAGE analysis revealed that the target gene was expressed at high levels at 0.6 mM concentration of IPTG for 24 h. The mouse polyclonal antibody against SV-A VP1 protein was produced and reached a high antiserum titer (1: 2,048,000). Immunized mice sera with the recombinant SV-A VP1 protein showed specific recognition of purified VP1 protein by western blot assay and could recognize native SV-A VP1 protein in PK-15 cells infected with SV-A by indirect immunofluorescence assay. The successfully purified recombinant protein was able to preserve its antigenic determinants and the generated mouse anti-SV-A VP1 antibodies could recognize native SV-A, which may have the potential to be used to detect SV-A infection in pigs.